E1B55_ADE40
ID E1B55_ADE40 Reviewed; 476 AA.
AC P10545;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 01-JUL-1989, sequence version 1.
DT 25-MAY-2022, entry version 76.
DE RecName: Full=E1B 55 kDa protein;
DE Short=E1B-55K;
DE AltName: Full=E1B protein, large T-antigen;
DE AltName: Full=E1B-495R;
OS Human adenovirus F serotype 40 (HAdV-40) (Human adenovirus 40).
OC Viruses; Varidnaviria; Bamfordvirae; Preplasmiviricota; Tectiliviricetes;
OC Rowavirales; Adenoviridae; Mastadenovirus; Human mastadenovirus F.
OX NCBI_TaxID=28284;
OH NCBI_TaxID=9606; Homo sapiens (Human).
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2961652; DOI=10.1016/0378-1119(87)90034-5;
RA van Loon A.E., Ligtenberg M., Reemst A.M.C.B., Sussenbach J.S.,
RA Rozijn T.H.;
RT "Structure and organization of the left-terminal DNA regions of fastidious
RT adenovirus types 40 and 41.";
RL Gene 58:109-126(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2968714; DOI=10.1016/0042-6822(88)90662-9;
RA Ishino M., Ohashi Y., Emoto T., Sawada Y., Fujinaga K.;
RT "Characterization of adenovirus type 40 E1 region.";
RL Virology 165:95-102(1988).
CC -!- FUNCTION: Plays a major role to prevent cellular inhibition of viral
CC genome replication. Assembles an SCF-like E3 ubiquitin ligase complex
CC based on the cellular proteins ELOB, ELOC, CUL5 and RBX1, in
CC cooperation with viral E4orf6. This viral RING-type ligase
CC ubiquitinates cellular substrates and targets them to proteasomal
CC degradation: TP53/p53, LIG4, MRE11-RAD50-NBS1 (MRN) complex, ITGA3,
CC DAXX and BLM. Degradation of host TP53/p53 activity is essential for
CC preventing E1A-induced TP53 accumulation that would otherwise lead to
CC cell apoptosis and growth arrest. E1B-55K also inactivates TP53
CC transcription-factor activity by binding its transactivation domain.
CC E1B-55K also functions as a SUMO1 E3 ligase for TP53 which causes the
CC latter to be sequestered in promyelocytic leukemia (PML) nuclear bodies
CC thereby contributing to maximal inhibition of TP53 function.
CC {ECO:0000250|UniProtKB:P03243}.
CC -!- SUBUNIT: Interacts with the transactivation domain of TP53 (via N-
CC terminus); this interaction leads to the inhibition of TP53 function
CC and/or its degradation. Interacts with host PML-4 and PML-5; this
CC interaction promotes efficient subnuclear targeting of E1B-55K to PML
CC nuclear bodies. Interacts with E4-ORF3 protein (By similarity)
CC Interacts with E4-ORF6 protein. Interacts with host DAXX protein; this
CC interaction might alterate the normal interactions of DAXX, PML, and
CC p53, which may contribute to cell transformation.
CC {ECO:0000250|UniProtKB:P03243, ECO:0000250|UniProtKB:P03244}.
CC -!- SUBCELLULAR LOCATION: Host nucleus {ECO:0000250|UniProtKB:P03243}. Host
CC cytoplasm {ECO:0000250|UniProtKB:P03243}. Note=Colocalizes with host
CC TP53 to host PML nuclear bodies. PML localization of E1B-55K is
CC necessary for E1B-55K-dependent SUMOylation of TP53.
CC {ECO:0000250|UniProtKB:P03243}.
CC -!- DOMAIN: Contains a PML interaction motif that allows the subnuclear PML
CC localization. {ECO:0000250|UniProtKB:P03243}.
CC -!- SIMILARITY: Belongs to the adenoviridae E1B 55 kDa protein family.
CC {ECO:0000305}.
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DR EMBL; M21276; AAA42444.1; -; Genomic_DNA.
DR EMBL; M18288; AAA42449.1; -; Genomic_RNA.
DR EMBL; L19443; AAC13958.1; -; Genomic_DNA.
DR PIR; C29195; WMADP6.
DR RefSeq; NP_040850.1; NC_001454.1.
DR SMR; P10545; -.
DR GeneID; 2715936; -.
DR KEGG; vg:2715936; -.
DR Proteomes; UP000151954; Genome.
DR GO; GO:0030430; C:host cell cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0042025; C:host cell nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0039526; P:modulation by virus of host apoptotic process; IEA:UniProtKB-KW.
DR InterPro; IPR006717; Adeno_E1B_55K_N.
DR InterPro; IPR002612; Adeno_E1B_55kDa.
DR InterPro; IPR011050; Pectin_lyase_fold/virulence.
DR Pfam; PF01696; Adeno_E1B_55K; 1.
DR Pfam; PF04623; Adeno_E1B_55K_N; 1.
DR SUPFAM; SSF51126; SSF51126; 1.
PE 3: Inferred from homology;
KW Early protein; Host cytoplasm; Host nucleus; Host-virus interaction;
KW Modulation of host cell apoptosis by virus; Reference proteome.
FT CHAIN 1..476
FT /note="E1B 55 kDa protein"
FT /id="PRO_0000221728"
FT REGION 1..20
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 42..95
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 70..84
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT CONFLICT 38
FT /note="A -> R (in Ref. 2; AAA42444)"
FT /evidence="ECO:0000305"
FT CONFLICT 53
FT /note="Missing (in Ref. 2; AAA42444)"
FT /evidence="ECO:0000305"
FT CONFLICT 448
FT /note="A -> T (in Ref. 2; AAA42444)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 476 AA; 52987 MW; E79028BDC548BEE7 CRC64;
MERPNSSVAG LYSGLHGNGS VENLATEEEG LRLLAGAASA RFGSSAGRGG GGGEPEGRPG
PFNGIVTEPD PEEGTSSGQR GGINGQRGTK RKMENEGEDF LKELTLSLMS RRHHESVWWA
DLEDEFKNGE MNLLYKYTFE QLKTHWLEAW EDFELALNTF AKVALRPDTI YTIKKTVNIR
KCAYVLGNGA VVRFQTCDRV AFNCAMQSLG PGLIGMSGVT FMNVRFVVEG FNGTVFASTT
QLTLHGVFFQ NCSGICVDSW GRVSARGCTF VACWKGVVGR NKSQMSVKKC VFERCIMAMV
VEGQARIRHN AGSDNVCFLL LKGTASVKHN MICGGGHSQL LTCADGNCQA LRVFHVVSHP
RRPWPVFEHN MLMRCTVHLG ARRGMFSPYQ SNFCHTKVLM ETDAFSRVWW NGVFDLTMEL
FKVVRYDESK VRCRPCECGA NHIRLYPATL NVTEQLRTDH QMMSCLRTDY ESSDED
